Structural and dynamics of apoA-1 mimetic peptide lipid nanodisc assemblies: A molecular dynamics study [0.03%]
一种模拟apoA-1肽的脂质纳米盘组件的结构和动力学研究——基于分子动力学方法
Rohith Ravi,Evgeniy S Salnikov,Burkhard Bechinger et al.
Rohith Ravi et al.
Apolipoprotein A-I (apoA-I) mimetic peptides, inspired by the principal protein component of high-density lipoprotein, self-assemble with lipids to form discoidal nanodiscs widely used in biomedical research and as versatile scaffolds for c...
Acylation of the RTX toxin MbxA stimulates host membrane disruption through a specific interaction with cholesterol [0.03%]
MbxA RTX 毒素的酰基化通过特异性结合胆固醇来刺激宿主细胞膜破裂
Feby Mariam Chacko,Sarah Michelle Ganz,Anne Pfitzer-Bilsing et al.
Feby Mariam Chacko et al.
RTX toxins (Repeat in ToXins) are pore-forming toxins secreted by gram-negative bacteria. They are known for their ability to disrupt host cell membranes, among which various human cells. The acylation of specific lysine residues in these t...
Nidhi Sorout,Volkhard Helms
Nidhi Sorout
The integral membrane pore Sec61 catalyzes the translocation of many secretory precursor proteins into the endoplasmic reticulum, as well as the insertion of transmembrane proteins into the cell and organellar membranes. Precursor proteins ...
Effect of amyloid-beta 1-40 and 1-42 peptides on the lateral diffusion and signaling of receptor for advanced glycation endproducts (RAGE) [0.03%]
Αβ肽对晚期糖基化终产物受体（RAGE）横向扩散及信号转导的影响研究
Chamari S Wijesooriya,Sharifur Rahman,Emily A Smith
Chamari S Wijesooriya
The receptor for advanced glycation endproducts (RAGE) is a pattern recognition receptor that interacts with different ligands, including the amyloid-beta (Aβ) peptides, to initiate signaling pathways and creates pro-inflammatory mediators...
Emad Ghazizadeh,Mahdi Zeidi,Wylie Stroberg
Emad Ghazizadeh
The endoplasmic reticulum (ER) is a highly dynamic organelle that undergoes continuous remodeling between tubular and sheet-like structures, driven by curvature-inducing proteins and membrane mechanics. Understanding the physical principles...
Bacterial cell susceptibility to the antimicrobial peptide MP1 depends on membrane lipid packing [0.03%]
细菌膜脂致密性决定抗菌肽MP1的杀菌活性
L Stefania Vargas-Velez,Florencia Hellriegel,Mariela R Monti et al.
L Stefania Vargas-Velez et al.
Polybia-MP1 is an antimicrobial peptide with broad-spectrum activity, but with varying efficacy against different bacterial strains. It is proposed to act on the cell membrane, and therefore, the higher tolerance of some strains may be attr...
Contribution to the special BBA issue dedicated to Joachim Seelig from lipid bilayers to the innate immune system [0.03%]
纪念Joachim Seelig的BBA特刊投稿：从脂质双层到先天免疫系统
Anna Seelig
Anna Seelig
This personal review in memory of Joachim Seelig covers half a century of membrane biophysics. The topics chosen give insight into the structure and function of our innate immune system, consisting in the membranes covering the external and...
Corrigendum to "Interaction of N-terminal peptide analogues of the Na+,K+-ATPase with membranes" [BBA Biomembr. 1860 (6) (2018) 1282-1291] [0.03%]
关于“Na +，K + -ATP酶N末端肽模拟物与膜的相互作用”的勘误（生物膜1860（6）（2018）1282-1291）
Khoa Nguyen,Alvaro Garcia,Marc-Antoine Sani et al.
Khoa Nguyen et al.
Reassessing DMSO-lipid interactions: Improved AMBER force fields emphasize solvent rather than bilayer effects in cryoprotection [0.03%]
重新评估DMSO-脂质相互作用：改进的AMBER力场强调溶剂而不是双层效应在冷冻保护中的作用
Ivan Klbik,Milan Melicherčík,Dušan Račko et al.
Ivan Klbik et al.
The interaction of dimethyl sulfoxide (DMSO) with lipid membranes has been extensively studied using molecular dynamics (MD) simulations, yet discrepancies with experimental findings persist. Here, we re-evaluate the effects of low DMSO con...
Corrigendum to "Unveiling the impact of membrane fluidity in shaping lipid-based drug delivery systems development." [Biochim. Biophys. Acta (BBA) - Biomembr. Volume 1868, Issue 1, January 2026, 184461] [0.03%]
关于“揭示膜流动性在脂质基药物传递系统开发中的影响”的勘误[BBA-生物膜卷1868期，2026年1月，184461]
Mariana Biscaia-Caleiras,Ana Sofia Lourenço,João Nuno Moreira et al.
Mariana Biscaia-Caleiras et al.